NIH-funded principal investigators at the University of Maryland-Baltimore have a pressing need for a variable-mode imaging system to quantitatively detect radio labeled, fluorescently-labeled, and chemifluorescent molecules. The Typhoon FLA 9000 Imaging System is an ideal instrument to meet the needs of our investigators. This instrument is a versatile workhorse for biomolecular imaging applications that supports a wide variety of sample formats. This instrument is requested to replace an aging imaging instrument that is now broken. Repair of this instrument is not feasible, since the repair cost is greater than the instrument value, the instrument is out-dated in terms of capability, and the company cannot guarantee available of parts in the future. The state-of-the-art capability of the Typhoon FLA 9000 instrument is necessary to meet the technology needs of 34 NIH grants (26 R01, 1 P01, 1 R03, 2 R21, 1 RC1, 1 R56, and 2 T32) awarded to 19 users at the UMB School of Medicine. In addition to the instrument, six phosphor screens and two software user licenses are requested to optimize data collection and analysis. The instrument will be housed in the existing Biochemistry and Molecular Biology Instrumentation Core (BMBIC). The BMBIC is designed to support the instrumentation needs of faculty in the northeast quadrant of the University of Maryland-Baltimore campus. The School of Medicine recently invested $400,000 to renovate and expand the BMBIC. The facility is managed by a BMBIC Oversight Committee and this committee directs the efforts of a technical assistant who manages the facility. Dr. Lu-Chang will be the primary faculty resource for technical issues associated with the present instrument. Cost of maintaining the service contract for this instrument will be shared by the School of Medicine, the University of Maryland Greenebaum Cancer Center and the Department of Biochemistry and Molecular Biology. The salary of the technical assistant is guaranteed by the Department of Biochemistry and Molecular Biology. A key long range research goal of all the users is to understand biological events at the molecular level as they pertain to human disease and cancer. The research programs cover multiple areas including protein-protein interaction, protein-nucleic acid interaction, DNA repair, transcriptional regulation, chromatin remodeling, epigenetic, cell signaling, stem-cell biology, and muscle cell physiology. Due to the malfunction of our aged phosphorimager, some of our research projects have suffered serious delays. The Typhoon FLA 9000 will substantially enhance the detection and quantitation of radiolabeled compounds essential for many researchers'experimental strategies, and will also provide investigators with a new fluorescence- and chemifluorescence-based detection platform that will enable them to meet the needs of their NIH-funded programs. Additionally, we believe it is important for students and postdoctoral associates to be trained with the state-of-the-art instrumentation. The new imaging system will enhance the training of students supported by five current NIH-funded graduate/postdoctoral training programs and the MD/PhD medical scientist training program.
| Hwang, Bor-Jang; Jin, Jin; Gunther, Randall et al. (2015) Association of the Rad9-Rad1-Hus1 checkpoint clamp with MYH DNA glycosylase and DNA. DNA Repair (Amst) 31:80-90 |
| Hwang, Bor-Jang; Jin, Jin; Gao, Ying et al. (2015) SIRT6 protein deacetylase interacts with MYH DNA glycosylase, APE1 endonuclease, and Rad9-Rad1-Hus1 checkpoint clamp. BMC Mol Biol 16:12 |
| Coey, Christopher T; Fitzgerald, Megan E; Maiti, Atanu et al. (2014) E2-mediated small ubiquitin-like modifier (SUMO) modification of thymine DNA glycosylase is efficient but not selective for the enzyme-product complex. J Biol Chem 289:15810-9 |
| Jin, Jin; Hwang, Bor-Jang; Chang, Po-Wen et al. (2014) Interaction of apurinic/apyrimidinic endonuclease 2 (Apn2) with Myh1 DNA glycosylase in fission yeast. DNA Repair (Amst) 15:1-10 |
| Hwang, Bor-Jang; Madabushi, Amrita; Jin, Jin et al. (2014) Histone/protein deacetylase SIRT1 is an anticancer therapeutic target. Am J Cancer Res 4:211-21 |
